ID A0A0Q0ZXG1_9SPHI Unreviewed; 959 AA.
AC A0A0Q0ZXG1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=AQF98_13175 {ECO:0000313|EMBL:KQC00425.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC00425.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQC00425.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQC00425.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQC00425.1}.
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DR EMBL; LLWP01000005; KQC00425.1; -; Genomic_DNA.
DR RefSeq; WP_055132414.1; NZ_LLWP01000005.1.
DR AlphaFoldDB; A0A0Q0ZXG1; -.
DR STRING; 1740090.AQF98_13175; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000050543; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR049315; GDC-P_N.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00461; gcvP; 1.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000050543}.
FT DOMAIN 13..437
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..734
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..895
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 703
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 959 AA; 104890 MW; B28BF76B30042C5E CRC64;
MSLNIHYQED FQDRHIAPNA EDTAAMLHTI GVKSIDELIE QTVPQKIRLK QPLNLPKAKS
EIEYLTSLKQ TASLNKVFKS YIGQGYYDTL TPGVILRNVM ENPGWYTQYT PYQAEIAQGR
LQALLNFQTM VIDLTGMEIA NASLLDEGTA AAEAMFMQYS LRKDQKATKY FVSDLIFAQT
IDILKTRANP FGIELVIGNH EQFTATEEFF GAIVQYPAGN GEVFDYTNFA ATLHSQNIKL
TVIADLLSLT LLTPPGEWGA DVVVGTTQRF GVPMGFGGPH AAYFATKDEY KRSIPGRIIG
VTIDSNDNYA LRMALQTREQ HIRRDKATSN ICTAQALLAI MAGFYAAYHG PKGLKKIAER
THGLTVSLAK SLAEIGYTVL SKSYFDTIQL DLGDLTGSIH KECLDNNINL NYNGNLVSIS
LDETTSFEDV KLLVRIFSKV KGISADSLNV IESVETTIPT NLQRTSAYLT HPVFNAHHSE
HEMLRYIKSL ETKDLSLCHS MIALGSCTMK LNATSEMIPV TWPEFGKVHP FAPADQVLGY
YTVFNELDKW LSEITGFAAM SLQPNAGAQG EYAGLMVIRA YHQDRGDFHR NIALIPASAH
GTNPASAAMA GMKIVVVKSL ENGNIDVEDL KAKAAEHAAN LSCLMVTYPS THGVFEESII
DICNIIHENG GQVYMDGANM NAQVGLTSPA NIGADVCHLN LHKTFCIPHG GGGPGMGPIG
VAAHLVKYLP GHAVVDINNE KSIPAVSSAP WGSASILIIS HAYIAMMGGE GLTDATKYAI
LNANYMKARL EAHYPVLYSG AQGRCAHEMI LDCRGFKNFG IEVVDIAKRL MDYGFHAPTV
SFPVAGTLMV EPTESEPKHE LDRFCDALIA IRNEISAVEN GSLDKTDNPL KNAPHTSAVV
TANEWTHGYS RQTAAFPLPY VAAYKFWPSV GRVNDSHGDR ALICACPPIE SYMEEEAIA
//
